Structural Studies of Amyloids by Quenched Hydrogen–Deuterium Exchange by NMR
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Author / Producer
Date
2012
Publication Type
Book Chapter
ETH Bibliography
yes
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Abstract
The elucidation of the structure of amyloid fi brils and related aggregates is an important step towards understanding the pathogenesis of diseases such as Alzheimer’s and Parkinson’s, which feature protein misfolding and/or aggregation. However, the large size and poor solubility of amyloid-like fibrils make them resistant to high-resolution structure determination. Here, we describe the use of hydrogen–deuterium exchange coupled with NMR as an indirect strategy to determine the folding regions of amyloid-forming proteins at residue level resolution.
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Publication status
published
Book title
Amyloid Proteins
Journal / series
Volume
849
Pages / Article No.
185 - 198
Publisher
Humana Press
Event
Edition / version
Methods
Software
Geographic location
Date collected
Date created
Subject
Amyloid fibrils; H/D exchange; NMR; Aβ, α-synuclein
Organisational unit
03782 - Riek, Roland / Riek, Roland